Protein:CD6 |
Protein Summary |
 Gene summary |
| Gene name: CD6 | ASpdb.0 ID: 923 | Gene | Gene symbol | CD6 | Gene ID | 923 |
| Gene name | CD6 molecule |
| Synonyms | TP120 |
| Cytomap | 11q12.2 |
| Type of gene | protein-coding |
| Description | T-cell differentiation antigen CD6CD6 antigenT12 |
| Modification date | 20240403 |
| UniProtAcc | P30203 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | CD6 | GO:0001530 | lipopolysaccharide binding | 17601777 |
| Gene | CD6 | GO:0001772 | immunological synapse | 15294938 |
| Gene | CD6 | GO:0002438 | acute inflammatory response to antigenic stimulus | 17601777 |
| Gene | CD6 | GO:0005886 | plasma membrane | 15294938 |
| Gene | CD6 | GO:0031663 | lipopolysaccharide-mediated signaling pathway | 17601777 |
| Gene | CD6 | GO:0032496 | response to lipopolysaccharide | 17601777 |
| Gene | CD6 | GO:0042101 | T cell receptor complex | 15294938 |
| Gene | CD6 | GO:1900017 | positive regulation of cytokine production involved in inflammatory response | 17601777 |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| P30203-1 | P30203-1_5a2e_A.pdb | 5A2E | X-ray | 3.15 | A | 43 | 364 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| P30203 | CD6 | P30203-1 | P30203-2 | 668 | 636 | 431 | 462 | Deletion | none | none | 430 | 430 |
| P30203 | CD6 | P30203-1 | P30203-3 | 668 | 595 | 431 | 462 | Deletion | none | none | 430 | 430 |
| P30203 | CD6 | P30203-1 | P30203-3 | 668 | 595 | 463 | 504 | Substitution | VFMLPIQVQAPPPEDSDSGSDSDYEHYDFSAQPPVALTTFYN | D | 431 | 431 |
| P30203 | CD6 | P30203-1 | P30203-4 | 668 | 601 | 431 | 462 | Deletion | none | none | 430 | 430 |
| P30203 | CD6 | P30203-1 | P30203-4 | 668 | 601 | 613 | 647 | Deletion | none | none | 580 | 580 |
| P30203 | CD6 | P30203-1 | P30203-5 | 668 | 592 | 463 | 504 | Substitution | VFMLPIQVQAPPPEDSDSGSDSDYEHYDFSAQPPVALTTFYN | D | 463 | 463 |
| P30203 | CD6 | P30203-1 | P30203-5 | 668 | 592 | 613 | 647 | Deletion | none | none | 571 | 571 |
| P30203 | CD6 | P30203-1 | P30203-6 | 668 | 545 | 261 | 383 | Deletion | none | none | 260 | 260 |
| P30203 | CD6 | P30203-1 | P30203-7 | 668 | 567 | 259 | 359 | Deletion | none | none | 258 | 258 |
| Multiple sequence alignment of our canonical and alternatively spliced CD6 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of CD6 |
| UniProt-id | ENSG | ENST | ENSP |
| P30203-1 | ENSG00000013725.14 | ENST00000313421.11 | ENSP00000323280.7 |
| P30203-4 | ENSG00000013725.14 | ENST00000352009.9 | ENSP00000340628.5 |
| P30203-5 | ENSG00000013725.14 | ENST00000452451.6 | ENSP00000390676.2 |
| UniProt-id | NM ID | NP ID |
| P30203-1 | NM_006725.4 | NP_006716.3 |
| P30203-4 | NM_001254750.1 | NP_001241679.1 |
| P30203-5 | NM_001254751.1 | NP_001241680.1 |
| P30203-7 | XM_011545362.1 | XP_011543664.1 |
| Amino acid sequences of our canonical and alternatively spliced CD6 |
| accession_id | Protein sequence |
| P30203-1 | MWLFFGITGLLTAALSGHPSPAPPDQLNTSSAESELWEPGERLPVRLTNGSSSCSGTVEVRLEASWEPACGALWDSRAAEAVCRALGCGG AEAASQLAPPTPELPPPPAAGNTSVAANATLAGAPALLCSGAEWRLCEVVEHACRSDGRRARVTCAENRALRLVDGGGACAGRVEMLEHG EWGSVCDDTWDLEDAHVVCRQLGCGWAVQALPGLHFTPGRGPIHRDQVNCSGAEAYLWDCPGLPGQHYCGHKEDAGAVCSEHQSWRLTGG ADRCEGQVEVHFRGVWNTVCDSEWYPSEAKVLCQSLGCGTAVERPKGLPHSLSGRMYYSCNGEELTLSNCSWRFNNSNLCSQSLAARVLC SASRSLHNLSTPEVPASVQTVTIESSVTVKIENKESRELMLLIPSIVLGILLLGSLIFIAFILLRIKGKYALPVMVNHQHLPTTIPAGSN SYQPVPITIPKEVFMLPIQVQAPPPEDSDSGSDSDYEHYDFSAQPPVALTTFYNSQRHRVTDEEVQQSRFQMPPLEEGLEELHASHIPTA NPGHCITDPPSLGPQYHPRSNSESSTSSGEDYCNSPKSKLPPWNPQVFSSERSSFLEQPPNLELAGTQPAFSAGPPADDSSSTSSGEWYQ |
| P30203-2 | MWLFFGITGLLTAALSGHPSPAPPDQLNTSSAESELWEPGERLPVRLTNGSSSCSGTVEVRLEASWEPACGALWDSRAAEAVCRALGCGG AEAASQLAPPTPELPPPPAAGNTSVAANATLAGAPALLCSGAEWRLCEVVEHACRSDGRRARVTCAENRALRLVDGGGACAGRVEMLEHG EWGSVCDDTWDLEDAHVVCRQLGCGWAVQALPGLHFTPGRGPIHRDQVNCSGAEAYLWDCPGLPGQHYCGHKEDAGAVCSEHQSWRLTGG ADRCEGQVEVHFRGVWNTVCDSEWYPSEAKVLCQSLGCGTAVERPKGLPHSLSGRMYYSCNGEELTLSNCSWRFNNSNLCSQSLAARVLC SASRSLHNLSTPEVPASVQTVTIESSVTVKIENKESRELMLLIPSIVLGILLLGSLIFIAFILLRIKGKYVFMLPIQVQAPPPEDSDSGS DSDYEHYDFSAQPPVALTTFYNSQRHRVTDEEVQQSRFQMPPLEEGLEELHASHIPTANPGHCITDPPSLGPQYHPRSNSESSTSSGEDY CNSPKSKLPPWNPQVFSSERSSFLEQPPNLELAGTQPAFSAGPPADDSSSTSSGEWYQNFQPPPQPPSEEQFGCPGSPSPQPDSTDNDDY |
| P30203-3 | MWLFFGITGLLTAALSGHPSPAPPDQLNTSSAESELWEPGERLPVRLTNGSSSCSGTVEVRLEASWEPACGALWDSRAAEAVCRALGCGG AEAASQLAPPTPELPPPPAAGNTSVAANATLAGAPALLCSGAEWRLCEVVEHACRSDGRRARVTCAENRALRLVDGGGACAGRVEMLEHG EWGSVCDDTWDLEDAHVVCRQLGCGWAVQALPGLHFTPGRGPIHRDQVNCSGAEAYLWDCPGLPGQHYCGHKEDAGAVCSEHQSWRLTGG ADRCEGQVEVHFRGVWNTVCDSEWYPSEAKVLCQSLGCGTAVERPKGLPHSLSGRMYYSCNGEELTLSNCSWRFNNSNLCSQSLAARVLC SASRSLHNLSTPEVPASVQTVTIESSVTVKIENKESRELMLLIPSIVLGILLLGSLIFIAFILLRIKGKYDSQRHRVTDEEVQQSRFQMP PLEEGLEELHASHIPTANPGHCITDPPSLGPQYHPRSNSESSTSSGEDYCNSPKSKLPPWNPQVFSSERSSFLEQPPNLELAGTQPAFSA |
| P30203-4 | MWLFFGITGLLTAALSGHPSPAPPDQLNTSSAESELWEPGERLPVRLTNGSSSCSGTVEVRLEASWEPACGALWDSRAAEAVCRALGCGG AEAASQLAPPTPELPPPPAAGNTSVAANATLAGAPALLCSGAEWRLCEVVEHACRSDGRRARVTCAENRALRLVDGGGACAGRVEMLEHG EWGSVCDDTWDLEDAHVVCRQLGCGWAVQALPGLHFTPGRGPIHRDQVNCSGAEAYLWDCPGLPGQHYCGHKEDAGAVCSEHQSWRLTGG ADRCEGQVEVHFRGVWNTVCDSEWYPSEAKVLCQSLGCGTAVERPKGLPHSLSGRMYYSCNGEELTLSNCSWRFNNSNLCSQSLAARVLC SASRSLHNLSTPEVPASVQTVTIESSVTVKIENKESRELMLLIPSIVLGILLLGSLIFIAFILLRIKGKYVFMLPIQVQAPPPEDSDSGS DSDYEHYDFSAQPPVALTTFYNSQRHRVTDEEVQQSRFQMPPLEEGLEELHASHIPTANPGHCITDPPSLGPQYHPRSNSESSTSSGEDY |
| P30203-5 | MWLFFGITGLLTAALSGHPSPAPPDQLNTSSAESELWEPGERLPVRLTNGSSSCSGTVEVRLEASWEPACGALWDSRAAEAVCRALGCGG AEAASQLAPPTPELPPPPAAGNTSVAANATLAGAPALLCSGAEWRLCEVVEHACRSDGRRARVTCAENRALRLVDGGGACAGRVEMLEHG EWGSVCDDTWDLEDAHVVCRQLGCGWAVQALPGLHFTPGRGPIHRDQVNCSGAEAYLWDCPGLPGQHYCGHKEDAGAVCSEHQSWRLTGG ADRCEGQVEVHFRGVWNTVCDSEWYPSEAKVLCQSLGCGTAVERPKGLPHSLSGRMYYSCNGEELTLSNCSWRFNNSNLCSQSLAARVLC SASRSLHNLSTPEVPASVQTVTIESSVTVKIENKESRELMLLIPSIVLGILLLGSLIFIAFILLRIKGKYALPVMVNHQHLPTTIPAGSN SYQPVPITIPKEDSQRHRVTDEEVQQSRFQMPPLEEGLEELHASHIPTANPGHCITDPPSLGPQYHPRSNSESSTSSGEDYCNSPKSKLP |
| P30203-6 | MWLFFGITGLLTAALSGHPSPAPPDQLNTSSAESELWEPGERLPVRLTNGSSSCSGTVEVRLEASWEPACGALWDSRAAEAVCRALGCGG AEAASQLAPPTPELPPPPAAGNTSVAANATLAGAPALLCSGAEWRLCEVVEHACRSDGRRARVTCAENRALRLVDGGGACAGRVEMLEHG EWGSVCDDTWDLEDAHVVCRQLGCGWAVQALPGLHFTPGRGPIHRDQVNCSGAEAYLWDCPGLPGQHYCGHKEDAGAVCSESSVTVKIEN KESRELMLLIPSIVLGILLLGSLIFIAFILLRIKGKYALPVMVNHQHLPTTIPAGSNSYQPVPITIPKEVFMLPIQVQAPPPEDSDSGSD SDYEHYDFSAQPPVALTTFYNSQRHRVTDEEVQQSRFQMPPLEEGLEELHASHIPTANPGHCITDPPSLGPQYHPRSNSESSTSSGEDYC NSPKSKLPPWNPQVFSSERSSFLEQPPNLELAGTQPAFSAGPPADDSSSTSSGEWYQNFQPPPQPPSEEQFGCPGSPSPQPDSTDNDDYD |
| P30203-7 | MWLFFGITGLLTAALSGHPSPAPPDQLNTSSAESELWEPGERLPVRLTNGSSSCSGTVEVRLEASWEPACGALWDSRAAEAVCRALGCGG AEAASQLAPPTPELPPPPAAGNTSVAANATLAGAPALLCSGAEWRLCEVVEHACRSDGRRARVTCAENRALRLVDGGGACAGRVEMLEHG EWGSVCDDTWDLEDAHVVCRQLGCGWAVQALPGLHFTPGRGPIHRDQVNCSGAEAYLWDCPGLPGQHYCGHKEDAGAVCSASRSLHNLST PEVPASVQTVTIESSVTVKIENKESRELMLLIPSIVLGILLLGSLIFIAFILLRIKGKYALPVMVNHQHLPTTIPAGSNSYQPVPITIPK EVFMLPIQVQAPPPEDSDSGSDSDYEHYDFSAQPPVALTTFYNSQRHRVTDEEVQQSRFQMPPLEEGLEELHASHIPTANPGHCITDPPS LGPQYHPRSNSESSTSSGEDYCNSPKSKLPPWNPQVFSSERSSFLEQPPNLELAGTQPAFSAGPPADDSSSTSSGEWYQNFQPPPQPPSE |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| CD6 (go to UniProt):P30203 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| P30203 | Topological domain | 18 | 402 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=261;End=383 |
| P30203 | Topological domain | 18 | 402 | Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=259;End=359 |
| P30203 | Topological domain | 424 | 668 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=431;End=462 |
| P30203 | Topological domain | 424 | 668 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=431;End=462 |
| P30203 | Topological domain | 424 | 668 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=463;End=504 |
| P30203 | Topological domain | 424 | 668 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=431;End=462 |
| P30203 | Topological domain | 424 | 668 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=613;End=647 |
| P30203 | Topological domain | 424 | 668 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=463;End=504 |
| P30203 | Topological domain | 424 | 668 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=613;End=647 |
| P30203 | Domain | 161 | 260 | Note=SRCR 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00196 | Type=Deletion;Start=259;End=359 |
| P30203 | Domain | 265 | 361 | Note=SRCR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00196 | Type=Deletion;Start=261;End=383 |
| P30203 | Domain | 265 | 361 | Note=SRCR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00196 | Type=Deletion;Start=259;End=359 |
| P30203 | Region | 471 | 490 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=463;End=504 |
| P30203 | Region | 471 | 490 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=463;End=504 |
| P30203 | Region | 537 | 668 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=613;End=647 |
| P30203 | Region | 537 | 668 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=613;End=647 |
| P30203 | Compositional bias | 614 | 631 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=613;End=647 |
| P30203 | Compositional bias | 614 | 631 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=613;End=647 |
Gene Isoform Structures and Expression Levels for CD6 |
| Gene structures of our canonical and alternative spliced genes of CD6 * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of P30203-1 |
| 3D view using mol* of P30203-2 |
| 3D view using mol* of P30203-3 |
| 3D view using mol* of P30203-4 |
| 3D view using mol* of P30203-5 |
| 3D view using mol* of P30203-6 |
| 3D view using mol* of P30203-7 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of P30203-1 |
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| pLDDT distribution across the protein length of P30203-2 |
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| pLDDT distribution across the protein length of P30203-3 |
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| pLDDT distribution across the protein length of P30203-4 |
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| pLDDT distribution across the protein length of P30203-5 |
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| pLDDT distribution across the protein length of P30203-6 |
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| pLDDT distribution across the protein length of P30203-7 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of P30203-1 |
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| Ramachandran plot of P30203-2 |
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| Ramachandran plot of P30203-3 |
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| Ramachandran plot of P30203-4 |
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| Ramachandran plot of P30203-5 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| P30203-1 | 1.007 | 229 | 1.045 | 796.789 | 0.624 | 0.67 | 0.876 | 0.517 | 0.911 | 0.567 | 1.511 | 166,171,187,188,189,190,191,192,196,206,207,208,20 9,210,211,212,215,216,258,262,264,281,283,284,285, 286,322,323,489,490,491,492,493,494,495,496,497,49 8,499,500,503,504,507,629,631,632,633,634,635 |
| P30203-2 | 1 | 222 | 1.013 | 1007.048 | 0.619 | 0.697 | 0.911 | 0.346 | 1.061 | 0.326 | 0.721 | 50,51,55,92,152,154,155,156,157,158,160,161,162,16 3,168,169,170,177,178,179,180,182,201,202,203,204, 236,238,261,262,263,265,282,336,338,339,340,342,54 2,543,544,546,547,548,549,550,551,552,553,555,556 |
| P30203-3 | 1.012 | 189 | 1.071 | 810.509 | 0.712 | 0.64 | 0.843 | 0.636 | 0.776 | 0.819 | 1.404 | 165,166,167,168,169,171,192,193,196,200,205,206,20 7,208,215,216,232,258,260,261,262,263,264,265,266, 267,273,283,284,306,307,336,338,342,501,503,505,50 7,508,510,511,512,513,514,515,561,562,563,564 |
| P30203-4 | 1.023 | 180 | 0.974 | 445.214 | 0.436 | 0.733 | 0.998 | 0.289 | 1.246 | 0.232 | 1.295 | 165,166,167,171,211,214,215,216,217,258,262,264,26 5,266,267,273,274,286,305,306,307,308,336,483,486, 487,488,489,490,491,492 |
| P30203-5 | 0.948 | 163 | 0.954 | 443.842 | 0.655 | 0.62 | 0.843 | 0.212 | 1.097 | 0.194 | 1.079 | 166,167,168,169,170,171,211,215,216,258,261,262,26 3,264,265,281,282,283,329,330,331,334,336,338,339, 340,341,342,343,344,346,523,524,525,526,527,531 |
| P30203-6 | 0.988 | 109 | 0.955 | 392.392 | 0.638 | 0.681 | 0.907 | 0.193 | 1.206 | 0.16 | 1.288 | 187,188,189,190,192,209,210,211,212,213,214,215,24 8,252,253,266,267,268,269,270,271,272,374,375,376, 377,378,380,381,384,385 |
| P30203-7 | 0.91 | 80 | 0.934 | 236.327 | 0.661 | 0.63 | 0.841 | 0.51 | 0.874 | 0.584 | 1.908 | 187,188,212,213,214,248,249,250,252,253,388,389,39 0,392,393,394,396,399,400,403,404,407 |
Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of P30203-1_P30203-1_5a2e_A.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P30203-1_5a2e_A_P30203-2.pdb |
| 3D view using mol* of P30203-1_5a2e_A_P30203-3.pdb |
| 3D view using mol* of P30203-1_5a2e_A_P30203-4.pdb |
| 3D view using mol* of P30203-1_5a2e_A_P30203-5.pdb |
| 3D view using mol* of P30203-1_5a2e_A_P30203-6.pdb |
| 3D view using mol* of P30203-1_5a2e_A_P30203-7.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P30203-1_P30203-2.pdb |
| 3D view using mol* of P30203-1_P30203-3.pdb |
| 3D view using mol* of P30203-1_P30203-4.pdb |
| 3D view using mol* of P30203-1_P30203-5.pdb |
| 3D view using mol* of P30203-1_P30203-6.pdb |
| 3D view using mol* of P30203-1_P30203-7.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/P30203-1_vs_P30203-2.png |
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| ./stats/secondary_structure/figure/P30203-1_vs_P30203-3.png |
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| ./stats/secondary_structure/figure/P30203-1_vs_P30203-4.png |
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| ./stats/secondary_structure/figure/P30203-1_vs_P30203-5.png |
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| ./stats/secondary_structure/figure/P30203-1_vs_P30203-6.png |
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| ./stats/secondary_structure/figure/P30203-1_vs_P30203-7.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/P30203-1_vs_P30203-2.png |
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| ./stats/relative_asa/P30203-1_vs_P30203-3.png |
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| ./stats/relative_asa/P30203-1_vs_P30203-4.png |
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| ./stats/relative_asa/P30203-1_vs_P30203-5.png |
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| ./stats/relative_asa/P30203-1_vs_P30203-6.png |
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| ./stats/relative_asa/P30203-1_vs_P30203-7.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to CD6 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to CD6 |
| Previous studies relating to the alternative splicing of CD6 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| CD6 | 26028048 | Tuning T Cell Activation: The Function of CD6 At the Immunological Synapse and in T Cell Responses. | CD6 immunotherapy to treat psoriasis and rheumatoid arthritis has reached the clinical trial stage with apparent success, and targeting CD6 with mAbs is being used in several animal models of autoimmunity and neuroinflammation with promising indications. However, the mode of action of the therapeutic CD6 mAbs is far from being understood, reflecting the uncertainties and controversy surrounding the mechanistic and biological functions of CD6. Initially regarded as a co-stimulatory receptor of T lymphocytes, recent studies suggest that CD6 can instead modulate early as well as late T cell responses. Also, opposing the contribution of CD6 adhesiveness in the establishment and stabilization of immunological synapses, the actual triggering of CD6 might induce anti-proliferative signals to the T lymphocyte. CD6 has an unusually long cytoplasmic tail and its gene undergoes peculiar patterns of activation-dependent alternative splicing that can on one hand determine whether or not the CD6 protein binds to its ligand, and on the other include or exclude intracellular sequences that may transduce positive or negative signaling. In this review we discuss the multiple aspects that determine the nature of the signals transmitted via CD6 and the context that may define a dual role for this important T cell surface molecule. | D007154 | Immune System Diseases |
Clinically important variants in CD6 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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